Title: Chaperone‐like activity of a synthetic peptide toward oxidized γ‐crystallin
Abstract: αA‐Crystallin can function like a molecular chaperone. We recently reported that the αA‐crystallin sequence, KFVIFLDVKHFSPEDLTVK (peptide‐1, residues 70–88) by itself possesses chaperone‐like (anti‐aggregating) activity during a thermal denaturation assay. Based on the above data we proposed that the peptide‐1 sequence was the functional site in αA‐crystallin. In this study we investigated the specificity of peptide‐1 against γ‐crystallin aggregation in the presence of H 2 O 2 and CuSO 4. Peptide‐1 was able to completely protect against the oxidation‐induced aggregation of γ‐crystallin. Removal of N‐terminal Lys or the replacement of Lys with Asp ( D FVIFLDVKHFSPEDLTVK, peptide‐2) did not alter the anti‐aggregation property of peptide‐1. However, deletion of KF residues from the N‐terminus of peptide‐1 resulted in a significant loss of its anti‐aggregation property. Bio‐gel P‐30 size‐exclusion chromatography of γ‐crystallin incubated with peptide‐2 under oxidative conditions revealed that a major portion of the peptide elutes in the void volume region along with γ‐crystallin, suggesting the binding of the peptide to the protein. Peptide‐1 and ‐2 were also able to prevent the UV‐induced aggregation of γ‐crystallin. These data indicate that the same amino acid sequence in αA‐crystallin is likely to be responsible for suppressing the heat‐denatured, oxidatively modified and UV‐induced aggregation of proteins.
Publication Year: 2000
Publication Date: 2000-09-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 24
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